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  • Title: Optimization, purification, and characterization of hydroxylamine oxidoreductase from Acinetobacter sp. Y1.
    Author: Liu Y, Yuan X, Liu Z.
    Journal: Biotechnol Appl Biochem; 2019 Jul; 66(4):494-501. PubMed ID: 30905079.
    Abstract:
    Hydroxylamine oxidoreductase (HAO) is a key enzyme involved in ammonium removal pathway. To further study the enzyme, HAO was purified from heterotrophic nitrifier Acinetobacter sp. Y1 and its property was investigated. Results of single-factor experiments showed that the optimal carbon source, nitrogen source, and C/N ratio were trisodium citrate, ammonium sulfate, and 14, respectively, with incubation time of 16 H. DEAE SefinoseTM FF anion-exchange chromatography was used to purify HAO, followed by SefinoseTM CL-6B gel filtration chromatography. SDS-PAGE revealed that a 47 kDa enzyme was purified successfully, with a purification fold of 7.32 and a recovery rate of 19.40%. The optimized enzyme activity of purified HAO was tested at pH 8.0 and 30 °C. The results showed that the activity was increased by 43.78% and 25.64% in the presence of 1 mM Fe2+ and Fe3+ , respectively. HAO activity was increased with the increase of Na+ and K+ , Mn2+ , Zn2+ , Cu2+ , Ca2+ , Ba2+ inhibited the HAO activity at three concentrations. In addition, HAO activity was activated by ethylenediaminetetraacetic acid at 0.4 mM, and a negative effect arose as the dose increased. The purified enzyme from Y1 is different from other reported HAOs. Further study should be conducted to investigate the enzyme.
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